Dipolar NMR relaxation of nonprotonated aromatic carbons in proteins. Structural and dynamical effects.

Abstract:

:The crystal structure and a 96-ps molecular dynamics simulation used to analyze structural and motional contributions to spin-lattice (T1) relaxation times of phenylalanine and tyrosine C gamma carbons of the pancreatic trypsin inhibitor. The H beta and H delta protons geminal to C gamma are calculated to account for approximately 80% of the dipolar relaxation for each residue. Experimental T1 values for the phenylalanine residues obtained at 25 MHz are observed to be 15-25% longer than estimates based on the rigid crystal structure. It is shown how an increase in T1 can be related to order parameters for the picosecond motional averaging of the important C,H dipolar interactions, and how these order parameters can be calculated from a protein molecular dynamics trajectory.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Levy RM,Dobson CM,Karplus M

doi

10.1016/S0006-3495(82)84496-2

subject

Has Abstract

pub_date

1982-07-01 00:00:00

pages

107-13

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(82)84496-2

journal_volume

39

pub_type

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